CDH2

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Cadherin 2, type 1, N-cadherin (neuronal)
Protein CDH2 PDB 1ncg.png
PDB rendering based on 1ncg.
Identifiers
Symbols CDH2 ; CD325; CDHN; CDw325; NCAD
External IDs OMIM114020 MGI88355 HomoloGene20424 ChEMBL: 1697669 GeneCards: CDH2 Gene
RNA expression pattern
PBB GE CDH2 203440 at tn.png
PBB GE CDH2 203441 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1000 12558
Ensembl ENSG00000170558 ENSMUSG00000024304
UniProt P19022 P15116
RefSeq (mRNA) NM_001792 NM_007664
RefSeq (protein) NP_001783 NP_031690
Location (UCSC) Chr 18:
25.53 – 25.76 Mb
Chr 18:
16.59 – 16.81 Mb
PubMed search [1] [2]

Cadherin-2 (CDH2), also known as neural cadherin (NCAD) is a protein that in humans is encoded by the CDH2 gene.[1][2] CDH2 has also been designated as CD325 (cluster of differentiation 325).

Function[edit]

Cadherin 2 a classical cadherin from the cadherin superfamily. Cadherin 2 is a calcium dependent cell-cell adhesion glycoprotein comprising five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. The protein functions during gastrulation and is required for establishment of left-right asymmetry. At certain central nervous system synapses, presynaptic to postsynaptic adhesion is mediated at least in part by this gene product.[3]

N-cadherins interact with catenins to play an important role in learning and memory (For full article see Cadherin-catenin complex in learning and memory).

Role in cancer metastasis[edit]

N-Cadherin is commonly found in cancer cells and provides a mechanism for transendothelial migration. When a cancer cell adheres to the endothelial cells of a blood vessel it up-regulates the src kinase pathway, which phosphorylates beta-catenins attached to both N-cadherin (this protein) and E-cadherins. This causes the intercellular connection between two adjacent endothelial cells to fail and allows the cancer cell to slip through.[4]

Interactions[edit]

CDH2 has been shown to interact with Beta-catenin,[5][6] Plakoglobin,[5][7] Catenin (cadherin-associated protein), alpha 1,[5][6] CTNND1,[5][6] LRRC7,[8] CDH11,[5] and type IIb RPTPs including PTPmu (PTPRM)[9][10] and PTPrho (PTPRT).[11]

References[edit]

  1. ^ Walsh FS, Barton CH, Putt W, Moore SE, Kelsell D, Spurr N, Goodfellow PN (September 1990). "N-cadherin gene maps to human chromosome 18 and is not linked to the E-cadherin gene". J. Neurochem. 55 (3): 805–12. doi:10.1111/j.1471-4159.1990.tb04563.x. PMID 2384753. 
  2. ^ Reid RA, Hemperly JJ (October 1990). "Human N-cadherin: nucleotide and deduced amino acid sequence". Nucleic Acids Res. 18 (19): 5896–5896. doi:10.1093/nar/18.19.5896. PMC 332345. PMID 2216790. 
  3. ^ "Entrez Gene: CDH2 cadherin 2, type 1, N-cadherin (neuronal)". 
  4. ^ Ramis-Conde I, Chaplain MA, Anderson AR, Drasdo D (2009). "Multi-scale modelling of cancer cell intravasation: the role of cadherins in metastasis". Phys Biol 6 (1): 016008. doi:10.1088/1478-3975/6/1/016008. PMID 19321920. 
  5. ^ a b c d e Straub, Beate K; Boda Judit; Kuhn Caecilia; Schnoelzer Martina; Korf Ulrike; Kempf Tore; Spring Herbert; Hatzfeld Mechthild; Franke Werner W (Dec 2003). "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells". J. Cell. Sci. (England) 116 (Pt 24): 4985–95. doi:10.1242/jcs.00815. ISSN 0021-9533. PMID 14625392. 
  6. ^ a b c Wahl, James K; Kim Young J; Cullen Janet M; Johnson Keith R; Wheelock Margaret J (May 2003). "N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane". J. Biol. Chem. (United States) 278 (19): 17269–76. doi:10.1074/jbc.M211452200. ISSN 0021-9258. PMID 12604612. 
  7. ^ Sacco, P A; McGranahan T M; Wheelock M J; Johnson K R (Aug 1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. (UNITED STATES) 270 (34): 20201–6. doi:10.1074/jbc.270.34.20201. ISSN 0021-9258. PMID 7650039. 
  8. ^ Izawa, Ichiro; Nishizawa Miwako; Ohtakara Kazuhiro; Inagaki Masaki (Feb 2002). "Densin-180 interacts with delta-catenin/neural plakophilin-related armadillo repeat protein at synapses". J. Biol. Chem. (United States) 277 (7): 5345–50. doi:10.1074/jbc.M110052200. ISSN 0021-9258. PMID 11729199. 
  9. ^ Brady-Kalnay SM, Rimm DL, Tonks NK (1995). "Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo.". J Cell Biol 130 (4): 977–86. doi:10.1083/jcb.130.4.977. PMC 2199947. PMID 7642713. 
  10. ^ Brady-Kalnay SM, Mourton T, Nixon JP, Pietz GE, Kinch M, Chen H et al. (1998). "Dynamic interaction of PTPmu with multiple cadherins in vivo.". J Cell Biol 141 (1): 287–96. doi:10.1083/jcb.141.1.287. PMC 2132733. PMID 9531566. 
  11. ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. doi:10.1016/j.brainres.2006.07.122. PMID 16973135. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.